The binding mechanism of benzophenone-type UV filters and human serum albumin: The role of site, number, and type of functional group substitutions

Ma, Junchao; Yang, Bing; Hu, Xiaojie; Gao, Yanzheng; Qin, Chao

doi:10.1016/j.envpol.2023.121342

Cited by 20 publications

(2 citation statements)

References 54 publications

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“…Figure 3 illustrates that the negative surface area of TBBPA (157.29 Å 2 ) is larger than that of TCBPA (143.55 Å 2 ). These differences arising from varying halogen substitutions lead to significant alterations in the molecular surface electrostatic potential, indicating that a more stable complex between HSA and TBBPA would be formed if the latter had a higher negative surface area [49]. This finding aligns with the observed increase in K a values.…”

Section: ∆G (Kj•molsupporting

confidence: 73%

Impacts of Halogen Substitutions on Bisphenol A Compounds Interaction with Human Serum Albumin: Exploring from Spectroscopic Techniques and Computer Simulations

Zhang,

Cai,

Chen

et al. 2023

IJMS

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Bisphenol A (BPA) is an endocrine-disrupting compound, and the binding mechanism of BPA with carrier proteins has drawn widespread attention. Halogen substitutions can significantly impact the properties of BPA, resulting in various effects for human health. Here, we selected tetrabromobisphenol A (TBBPA) and tetrachlorobisphenol A (TCBPA) to investigate the interaction between different halogen-substituted BPAs and human serum albumin (HSA). TBBPA/TCBPA spontaneously occupied site I and formed stable binary complexes with HSA. Compared to TCBPA, TBBPA has higher binding affinity to HSA. The effect of different halogen substituents on the negatively charged surface area of BPA was an important reason for the higher binding affinity of TBBPA to HSA compared to TCBPA. Hydrogen bonds and van der Waals forces were crucial in the TCBPA–HSA complex, while the main driving factor for the formation of the TBBPA–HSA complex was hydrophobic interactions. Moreover, the presence of TBBPA/TCBPA changed the secondary structure of HSA. Amino acid residues such as Lys199, Lys195, Phe211, Arg218, His242, Leu481, and Trp214 were found to play crucial roles in the binding process between BPA compounds and HSA. Furthermore, the presence of halogen substituents facilitated the binding of BPA compounds with HSA.

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Section: ∆G (Kj•molsupporting

confidence: 73%

Impacts of Halogen Substitutions on Bisphenol A Compounds Interaction with Human Serum Albumin: Exploring from Spectroscopic Techniques and Computer Simulations

Zhang,

Cai,

Chen

et al. 2023

IJMS

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“…Estradiol is crucial for reproductive health and has other effects such as anti-inflammatory and neuroprotective properties. As a prominent protein in blood plasma, human serum albumin (HSA) is essential for the transport of numerous molecules throughout the body [ 16 , 17 , 18 ]. HSA has different binding sites that interact with various compounds, including fatty acids, hormones, and drugs [ 19 , 20 ].…”

Section: Introductionmentioning

confidence: 99%

Exploration of Binding Affinities of a 3β,6β-Diacetoxy-5α-cholestan-5-ol with Human Serum Albumin: Insights from Synthesis, Characterization, Crystal Structure, Antioxidant and Molecular Docking

Alam

2023

Molecules

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The present study describes the synthesis, characterization, and in vitro molecular interactions of a steroid 3β,6β-diacetoxy-5α-cholestan-5-ol. Through conventional and solid-state methods, a cholestane derivative was successfully synthesized, and a variety of analytical techniques were employed to confirm its identity, including high-resolution mass spectrometry (HRMS), Fourier transforms infrared (FT-IR), nuclear magnetic resonance (NMR), elemental analysis, and X-ray single-crystal diffraction. Optimizing the geometry of the steroid was undertaken using density functional theory (DFT), and the results showed great concordance with the data from the experiments. Fluorescence spectral methods and ultraviolet–vis absorption titration were employed to study the in vitro molecular interaction of the steroid regarding human serum albumin (HSA). The Stern-Volmer, modified Stern-Volmer, and thermodynamic parameters’ findings showed that steroids had a significant binding affinity to HSA and were further investigated by molecular docking studies to understand the participation of active amino acids in forming non-bonding interactions with steroids. Fluorescence studies have shown that compound 3 interacts with human serum albumin (HSA) through a static quenching mechanism. The binding affinity of compound 3 for HSA was found to be 3.18 × 104 mol−1, and the Gibbs free energy change (ΔG) for the binding reaction was −9.86 kcal mol−1 at 298 K. This indicates that the binding of compound 3 to HSA is thermodynamically favorable. The thermodynamic parameters as well as the binding score obtained from molecular docking at various Sudlow’s sites was −8.2, −8.5, and −8.6 kcal/mol for Sites I, II, and III, respectively, supporting the system’s spontaneity. Aside from its structural properties, the steroid demonstrated noteworthy antioxidant activity, as evidenced by its IC50 value of 58.5 μM, which is comparable to that of ascorbic acid. The findings presented here contribute to a better understanding of the pharmacodynamics of steroids.

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Environmental health risks induced by interaction between phthalic acid esters (PAEs) and biological macromolecules: A review

Wang

et al. 2023

Chemosphere

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The binding mechanism of benzophenone-type UV filters and human serum albumin: The role of site, number, and type of functional group substitutions

Cited by 20 publications

References 54 publications

Impacts of Halogen Substitutions on Bisphenol A Compounds Interaction with Human Serum Albumin: Exploring from Spectroscopic Techniques and Computer Simulations

Impacts of Halogen Substitutions on Bisphenol A Compounds Interaction with Human Serum Albumin: Exploring from Spectroscopic Techniques and Computer Simulations

Exploration of Binding Affinities of a 3β,6β-Diacetoxy-5α-cholestan-5-ol with Human Serum Albumin: Insights from Synthesis, Characterization, Crystal Structure, Antioxidant and Molecular Docking

Environmental health risks induced by interaction between phthalic acid esters (PAEs) and biological macromolecules: A review

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